Download MendeleyThe crystal structure of Escherichia coli MoeA, a protein from the molybdopterin synthesis pathway.
Schrag, J.D., Huang, W., Sivaraman, J., Smith, C., Plamondon, J., Larocque, R., Matte, A., Cygler, M.(2001) J Mol Biol 310: 419-431
- PubMed: 11428898
- DOI: https://doi.org/10.1006/jmbi.2001.4771
- Primary Citation of Related Structures:
1FC5 - PubMed Abstract:
MoeA is involved in synthesis of the molybdopterin cofactor, although its function is not yet clearly defined. The three-dimensional structure of the Escherichia coli protein was solved at 2.2 A resolution. The locations of highly conserved residues among the prokaryotic and eukaryotic MoeA homologs identifies a cleft in the dimer interface as the likely functional site. Of the four domains of MoeA, domain 2 displays a novel fold and domains 1 and 4 each have only one known structural homolog. Domain 3, in contrast, is structurally similar to many other proteins. The protein that resembles domain 3 most closely is MogA, another protein required for molybdopterin cofactor synthesis. The overall similarity between MoeA and MogA, and the similarities in a constellation of residues that are strongly conserved in MoeA, suggests that these proteins bind similar ligands or substrates and may have similar functions.
Organizational Affiliation:
Biotechnology Research Institute, National Research Council of Canada, 6100 Royalmount Avenue, Montreal, PQ, Canada. joe@bri.nrc.ca
